When unphosphorylated, dematin's two F-actin binding domains move independent of one another permitting them to bind different F-actin filaments.

the headpiece domain of dematin regulates calcium mobilization and signaling in platelets

a novel functional role for dematin in regulating erythrocyte membrane function.

Fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin headpiece C-terminal. The reduction of mobility in the loop region upon the S74E mutation can be seen from the (15)N order parameters.

results suggest that phosphorylation of the dematin headpiece acts as a conformational switch within this headpiece domain

a crucial role for this proline residue in structural stability and folding potential of HP (sub)domains consistent with Pro-Trp stacking as a more general determinant of protein stability

study investigated motions in the backbone of dematin headpiece domain and its mutant DHPS74E using several complementary NMR relaxation techniques

results suggest that the core domain of dematin exhibits properties typical of a natively unfolded protein, while the headpiece domain is folded in a conformation essentially identical to its native structure

results demonstrate that dematin plays a critical role in maintaining the fundamental properties of the membrane cytoskeleton complex.

the headpiece domain of dematin regulates calcium mobilization and signaling in platelets

remodeling of the host cell directed Plasmodium includes the recruitment of dematin, an actin-binding protein of the erythrocyte membrane skeleton and its repositioning to the parasite

physiological significance of dematin and demonstrate a role for the headpiece domain in the maintenance of structural integrity and mechanical properties of erythrocytes in vivo.

Dematin plays an essential role in the maintenance of erythrocyte shape and membrane stability; dematin-membrane interaction could link the junctional complex to the plasma membrane in erythroid cells.

Beschreibung des Gens

Dematin, or EPB49, is an actin-bundling protein originally identified in the erythroid membrane skeleton. Its actin-bundling activity is abolished upon phosphorylation by cAMP-dependent protein kinase and is restored after dephosphorylation (Rana et al., 1993